Q62005 · ZP1_MOUSE

  • Protein
    Zona pellucida sperm-binding protein 1
  • Gene
    Zp1
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Component of the zona pellucida, an extracellular matrix surrounding oocytes which mediates sperm binding, induction of the acrosome reaction and prevents post-fertilization polyspermy. The zona pellucida is composed of 3 to 4 glycoproteins, ZP1, ZP2, ZP3, and ZP4. ZP1 ensures the structural integrity of the zona pellucida.

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcollagen-containing extracellular matrix
Cellular Componentegg coat
Cellular Componentextracellular region
Cellular Componentplasma membrane
Molecular Functionstructural constituent of egg coat
Biological Processsingle fertilization

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

Gene names

    • Name
      Zp1

Organism names

  • Taxonomic identifier
  • Strains
    • NIH Swiss
    • 129/Sv
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    Q62005
  • Secondary accessions
    • Q62016

Proteomes

Organism-specific databases

Subcellular Location

Cell membrane
; Single-pass type I membrane protein

Processed zona pellucida sperm-binding protein 1

Zona pellucida

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain21-590Extracellular
Transmembrane591-611Helical
Topological domain612-623Cytoplasmic

Keywords

PTM/Processing

Features

Showing features for signal, chain, modified residue, glycosylation, disulfide bond, propeptide.

TypeIDPosition(s)Description
Signal1-20
ChainPRO_000030455421-?Processed zona pellucida sperm-binding protein 1
Modified residue21Pyrrolidone carboxylic acid
ChainPRO_000004167921-546Zona pellucida sperm-binding protein 1
Glycosylation49N-linked (GlcNAc...) asparagine
Glycosylation68N-linked (GlcNAc...) asparagine
Disulfide bond228↔253
Disulfide bond237↔252
Glycosylation240N-linked (GlcNAc...) asparagine
Disulfide bond247↔262
Glycosylation371N-linked (GlcNAc...) asparagine
Disulfide bond449↔470
PropeptidePRO_0000041680547-623Removed in mature form
Glycosylation554N-linked (GlcNAc...) asparagine
Glycosylation585N-linked (GlcNAc...) asparagine

Post-translational modification

Proteolytically cleaved before the transmembrane segment to yield the secreted ectodomain incorporated in the zona pellucida.
O-glycosylated.

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Expressed in oocytes.

Developmental stage

Not detected in resting oocytes. As oocytes begin to grow, levels increase to reach a maximum in midsized oocytes. Levels decrease in later stages of oocyte growth.

Gene expression databases

Interaction

Subunit

Polymers of ZP2 and ZP3 organized into long filaments cross-linked by ZP1 homodimers. Interacts with ZP3.

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region182-201Disordered
Domain226-266P-type
Domain271-542ZP

Domain

The ZP domain is involved in the polymerization of the ZP proteins to form the zona pellucida.

Sequence similarities

Belongs to the ZP domain family. ZPB subfamily.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    623
  • Mass (Da)
    68,723
  • Last updated
    1996-11-01 v1
  • Checksum
    9D95B8613B3B95C8
MAWGCFVVLLLLAAAPLRLGQRLHLEPGFEYSYDCGVRGMQLLVFPRPNQTVQFKVLDEFGNRFEVNNCSICYHWVTSEAQEHTVFSADYKGCHVLEKDGRFHLRVFIQAVLPNGRVDIAQDVTLICPKPDHTVTPDPYLAPPTTPEPFTPHAFALHPIPDHTLAGSGHTGLTTLYPEQSFIHPTPAPPSLGPGPAGSTVPHSQWGTLEPWELTELDSVGTHLPQERCQVASGHIPCMVNGSSKETCQQAGCCYDSTKEEPCYYGNTVTLQCFKSGYFTLVMSQETALTHGVLLDNVHLAYAPNGCPPTQKTSAFVVFHVPLTLCGTAIQVVGEQLIYENQLVSDIDVQKGPQGSITRDSAFRLHVRCIFNASDFLPIQASIFSPQPPAPVTQSGPLRLELRIATDKTFSSYYQGSDYPLVRLLREPVYVEVRLLQRTDPSLVLVLHQCWATPTTSPFEQPQWPILSDGCPFKGDNYRTQVVAADREALPFWSHYQRFTITTFMLLDSSSQNALRGQVYFFCSASACHPLGSDTCSTTCDSGIARRRRSSGHHNITLRALDIVSSPGAVGFEDAAKLEPSGSSRNSSSRMLLLLLAITLALAAGIFVGLIWAWAQKLWEGIRY

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
F7CW32F7CW32_MOUSEZp195

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict246in Ref. 1; AAC48480
Sequence conflict445in Ref. 1; AAC48480
Sequence conflict486in Ref. 1; AAC48480

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
U24230
EMBL· GenBank· DDBJ
AAB60507.1
EMBL· GenBank· DDBJ
Genomic DNA
U24227
EMBL· GenBank· DDBJ
AAB60507.1
EMBL· GenBank· DDBJ
Genomic DNA
U24228
EMBL· GenBank· DDBJ
AAB60507.1
EMBL· GenBank· DDBJ
Genomic DNA
U24229
EMBL· GenBank· DDBJ
AAB60507.1
EMBL· GenBank· DDBJ
Genomic DNA
U20448
EMBL· GenBank· DDBJ
AAC48480.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

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